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- Title
Designing a Humanized Immunotoxin Based on HER2 Specific scFv and DFF40 Toxin Against Breast Cancer: An In-Silico Study.
- Authors
Movahedpour, Ahmad; Ahmadi, Khadijeh; Taheri-Anganeh, Mortaza; Amiri, Ahmad; Ahmadi, Nahid; Khatami, Seyyed Hossein; Zafaranchi z.m, Sara; Soltani Fard, Elahe; Moazamfard, Mostafa; Ghasemi, Hassan; Nezafat, Navid
- Abstract
Breast cancer is the most frequent cancer in women worldwide. Human epidermal growth factor receptor 2 (HER2) is a receptor which is overexpressed in breast cancer cells. Targeting this receptor could be a key factor for treatment of breast cancer patients. Herceptin is an antibody which can bind to HER2 receptor, in addition Herceptin derived single chain fragment V (scFv) can be used in designing immunotoxin for targeting HER2 positive cancer cells. DFF40 is a nuclease activated by caspase-3 and responsible for genomic DNA fragmentation during apoptosis. In this study, we used bioinformatics tools to design an immunotoxin containing HER2 specific scFv and DFF40 toxin. An immunotoxin construct was designed by linking scFv and DFF40 amino acids sequence via a peptide linker. The secondary structure, physicochemical features, solubility, and allergenicity of construct were predicted. The tertiary structure was built, refined, and evaluated. Protein–protein docking, and molecular dynamics studies were carried out for evaluation of immunotoxin-receptor binding, and the stability of the immunotoxin, respectively. The results indicated that the designed construct could be a stable protein with appropriate solubility, which is not an allergen and has a suitable structure which can bind to HER2 appropriately. Finally, this construct could be a promising candidate for producing an HER2 targeting immunotoxin. However, different in vitro and in vivo immunological assays should be performed to confirm the efficacy of the designed construct.
- Publication
International Journal of Peptide Research & Therapeutics, 2022, Vol 28, Issue 5, p1
- ISSN
1573-3149
- Publication type
Article
- DOI
10.1007/s10989-022-10443-9